Evidence map›Paper›PMID 35424159›Full record

ArticleRSC advances2021

Improvement of protein emulsion stability through glycosylated black bean protein covalent interaction with (-)-epigallocatechin-3-gallate.

Jubing Wang, Huanyu Zheng, Shenyi Zhang, Jishu Li, Xiuqing Zhu, Hua Jin, Jing Xu

Open access · goldAbstract read
In one paragraph

Article in RSC advances, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
6.4field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed, 55 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Jubing WangCollege of Art and Science, Northeast Agricultural University 150030 Harbin Heilongjiang PR China 15663431982@163.com zsylq123@163.com ljswy123@163.com jinhua@neau.edu.cn xujing@neau.edu.cn.
Huanyu ZhengCollege of Food Science, Northeast Agricultural University Harbin 150030 Heilongjiang China zhenghuanyu1@163.com.
Shenyi ZhangCollege of Art and Science, Northeast Agricultural University 150030 Harbin Heilongjiang PR China 15663431982@163.com zsylq123@163.com ljswy123@163.com jinhua@neau.edu.cn xujing@neau.edu.cn.
Jishu LiCollege of Art and Science, Northeast Agricultural University 150030 Harbin Heilongjiang PR China 15663431982@163.com zsylq123@163.com ljswy123@163.com jinhua@neau.edu.cn xujing@neau.edu.cn.
Xiuqing ZhuKey Laboratory of Grain Food and Comprehensive Processing of Grain Resource of Heilongjiang Province, College of Food Engineering, Harbin University of Commerce Harbin 150076 China xqzhuwang@163.com.
Hua JinCollege of Art and Science, Northeast Agricultural University 150030 Harbin Heilongjiang PR China 15663431982@163.com zsylq123@163.com ljswy123@163.com jinhua@neau.edu.cn xujing@neau.edu.cn.
Jing XuCollege of Art and Science, Northeast Agricultural University 150030 Harbin Heilongjiang PR China 15663431982@163.com zsylq123@163.com ljswy123@163.com jinhua@neau.edu.cn xujing@neau.edu.cn.ORCID https://orcid.org/0000-0002-5200-1166
Northeast Agricultural University · CNHarbin University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This study investigated the effects of covalent conjugates combined by glycosylated black bean protein isolate (BBPI-G) and (-)-epigallocatechin-3-gallate (EGCG) on the emulsion stability. Fourier transform infrared (FTIR) spectroscopy showed that covalent binding of EGCG with BBPI-G made the protein molecule unfolded. Besides, the emulsifying properties of BBPI-G were increased after combined with EGCG. BBPI-G-EGCG emulsion had lower mean particle size and higher content of interfacial protein adsorption (AP), which resulted in thicker and more impact oil-water interface. Therefore, the stability of emulsions was significantly improved. Furthermore, the emulsions prepared by BBPI-G-EGCG compounds exhibited considerable stability in storage, oxidation, thermal treatments, freeze-thaw and freeze-dried powders resolubility. This study demonstrated that the covalent bond of glycosylated protein and polyphenols could advance the emulsifying performance of protein, and BBPI-G-EGCG covalent complex was an effective emulsifier for preparing high stability emulsions.

Identifiers

PMID35424159
PMCPMC8693753
OpenAlexW3120187279

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.